6533b829fe1ef96bd128a573
RESEARCH PRODUCT
Expression and glycosylation studies of human FGF receptor 4
Marko UutelaAdrian GoldmanPirkko HeikinheimoChristian Oker-blomKari KatajaBritt-marie LooHeidi TuominenMarkku Jalkanensubject
Protein FoldingGlycosylationGlycosylationBlotting WesternImmunoblottingMolecular Sequence DataProtein RenaturationBiologyFibroblast growth factorMass SpectrometryInclusion bodiesCell Line03 medical and health scienceschemistry.chemical_compoundSDG 3 - Good Health and Well-beingEscherichia coliAnimalsHumansReceptor Fibroblast Growth Factor Type 4TrypsinAmino Acid SequenceDisulfidesReceptorChromatography High Pressure Liquid030304 developmental biologyInclusion Bodies0303 health sciencesHeparin030302 biochemistry & molecular biologyFibroblast growth factor receptor 4Fibroblast growth factor receptor 3Receptors Fibroblast Growth FactorMolecular biologyRecombinant Proteins3. Good healthchemistryFibroblast growth factor receptorMutationRNA splicing/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingBaculoviridaeBiotechnologydescription
Fibroblast growth factor receptor subtype 4 (FGFR4) has been shown to have special activation properties and just one splicing form, unlike the other FGFRs. FGFR4 overexpression is correlated with breast cancer and therefore FGFR4 is a target for drug design. Our aim is to overexpress high amounts of homogeneous FGFR4 extracellular domain (FGFR4ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4ed is glycosylated on three (N88, N234, and N266) of the six possible N-glycosylation sites but is not O-glycosylated. The deglycosylated triple mutant was expressed and had binding properties similar to those of glycosylated FGFR4ed, but was still heterogeneous. Large amounts of FGFR4ed have been produced into inclusion bodies in Escherichia coli and refolded at least partly correctly but the refolded E. coli-produced FGFR4ed still aggregates.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2001-01-01 |